Analyses of Protein Folding Codon affecting protein functions

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Synchronized translation, which enables time-course analyses of translation elongation, was constructed using in vitro translation system. The synchronized translation revealed that rare codons and stable RNA structures in open reading frame of mRNA temporarily stall the translation elongation. Contribution of protein binding to thermostability of particular nucleic acid structure was quantitatively evaluated under molecular crowding condition. Results from these analyses indicate that stabilities of mRNA structures possibly affect not only translation elongation process but also folding process of nascent proteins. In addition, correlation of thermostability of nascent mRNA structure and transcription efficiency was revealed by analyses of in vitro transcription.